ID   KEX1_CRYGW              Reviewed;         687 AA.
AC   E6R6G5;
DT   27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT   08-MAR-2011, sequence version 1.
DT   22-FEB-2023, entry version 50.
DE   RecName: Full=Pheromone-processing carboxypeptidase KEX1;
DE            EC=3.4.16.6;
DE   AltName: Full=Carboxypeptidase D;
DE   Flags: Precursor;
GN   Name=KEX1; OrderedLocusNames=CGB_E0630W;
OS   Cryptococcus gattii serotype B (strain WM276 / ATCC MYA-4071)
OS   (Filobasidiella gattii) (Cryptococcus bacillisporus).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC   Tremellales; Cryptococcaceae; Cryptococcus;
OC   Cryptococcus gattii species complex.
OX   NCBI_TaxID=367775;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WM276 / ATCC MYA-4071;
RX   PubMed=21304167; DOI=10.1128/mbio.00342-10;
RA   D'Souza C.A., Kronstad J.W., Taylor G., Warren R., Yuen M., Hu G.,
RA   Jung W.H., Sham A., Kidd S.E., Tangen K., Lee N., Zeilmaker T., Sawkins J.,
RA   McVicker G., Shah S., Gnerre S., Griggs A., Zeng Q., Bartlett K., Li W.,
RA   Wang X., Heitman J., Stajich J.E., Fraser J.A., Meyer W., Carter D.,
RA   Schein J., Krzywinski M., Kwon-Chung K.J., Varma A., Wang J., Brunham R.,
RA   Fyfe M., Ouellette B.F.F., Siddiqui A., Marra M., Jones S., Holt R.,
RA   Birren B.W., Galagan J.E., Cuomo C.A.;
RT   "Genome variation in Cryptococcus gattii, an emerging pathogen of
RT   immunocompetent hosts.";
RL   MBio 2:E342-E342(2011).
CC   -!- FUNCTION: Protease with a carboxypeptidase B-like function involved in
CC       the C-terminal processing of the lysine and arginine residues from
CC       protein precursors. Promotes cell fusion and is involved in the
CC       programmed cell death (By similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Preferential release of a C-terminal arginine or lysine
CC         residue.; EC=3.4.16.6;
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network membrane
CC       {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the peptidase S10 family. {ECO:0000305}.
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DR   EMBL; CP000290; ADV22286.1; -; Genomic_DNA.
DR   RefSeq; XP_003194073.1; XM_003194025.1.
DR   AlphaFoldDB; E6R6G5; -.
DR   SMR; E6R6G5; -.
DR   ESTHER; crygw-kex1; Carboxypeptidase_S10.
DR   MEROPS; S10.007; -.
DR   GlyCosmos; E6R6G5; 2 sites, No reported glycans.
DR   GeneID; 10190080; -.
DR   KEGG; cgi:CGB_E0630W; -.
DR   VEuPathDB; FungiDB:CGB_E0630W; -.
DR   eggNOG; KOG1282; Eukaryota.
DR   HOGENOM; CLU_008523_11_1_1; -.
DR   OrthoDB; 1647009at2759; -.
DR   Proteomes; UP000007805; Chromosome E.
DR   GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0004185; F:serine-type carboxypeptidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR001563; Peptidase_S10.
DR   PANTHER; PTHR11802:SF190; PHEROMONE-PROCESSING CARBOXYPEPTIDASE KEX1; 1.
DR   PANTHER; PTHR11802; SERINE PROTEASE FAMILY S10 SERINE CARBOXYPEPTIDASE; 1.
DR   Pfam; PF00450; Peptidase_S10; 1.
DR   PRINTS; PR00724; CRBOXYPTASEC.
DR   SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
PE   3: Inferred from homology;
KW   Apoptosis; Carboxypeptidase; Glycoprotein; Golgi apparatus; Hydrolase;
KW   Membrane; Protease; Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL          1..?
FT                   /evidence="ECO:0000255"
FT   CHAIN           ?..687
FT                   /note="Pheromone-processing carboxypeptidase KEX1"
FT                   /id="PRO_0000411918"
FT   TOPO_DOM        ?..573
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        574..594
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        595..687
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REGION          1..55
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          610..671
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        613..641
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        652..671
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        226
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        446
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        503
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        471
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        480
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   687 AA;  76275 MW;  F6E945C8D8CB3B77 CRC64;
     MSGNDARARV RSLPSTSSPL ETRDSDEQES SSSQSQRGSR KRGPQRRATE LPSAADLYVP
     SLPGLPDMAT HPTHPLNIYA GMLPSYPGEG KVGGEGETGK DAKLYFLMAK ARRNAGKERV
     IFWFNGGPGC SSFDGSLMEV GPFRTVPASE TTTGMVEAKL VEGGWEEFAT VVFVDQPPGT
     GYSYAATNGY LHDFDELSAH FIEFLQNFYT VFPELKGVDT YLAGESFAGQ YIPFFADALI
     NSAELPNFPL KGIAIGNGWI DPKEQYPGYV EFAYEKGLID SGTPVSAAFV DLHKERADQM
     LTDQEAEEME AALKRCQEEM DKYTDPFTTP VNIDHCGEVM DSVTRPFTQE LNGKKVCMNV
     YDVRLVDDFP ACGMNWPPDL PDVYTFLRQD EVISALHASS KETAWVECNN KVSYELNLKH
     SHMSAALLPS ILEAGVPILM FAGAEDLICN YKGIERIVNG LEWGGEKGFA NATSQEWYLN
     GTQVGTWQTS RGLSYAKIFD SSHMVGFDVP HVTNDMIMRF MDVDVSLLPG MISQWSSRIG
     DDERTMIHVG DAGEAGGVPL IKGGNTDWEA WYNAVFAFLV LGILVSIVGL YFYFRRKPVS
     YRSRIALKQR GRHRQSHDRD EGDTAERMPL GSERLELDDI ERAEGYEFDD RDDEGYSGKG
     KGKGKELADD REEVMFALGD DDEDDRH
//